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PROTEINS

Structure, physiological role,

digestion, absorption, transportation,
utilisation, dietary sources,
requirements

Introduction
• are the most abundant nitrogen-containing compounds
in diet and the body
• are one of complex biomolecules in cells and tissues
(others lipids, DNA, RNA, polysaccharides)
• are large, complex and diverse compounds composed
of a long chain of amino acids, joined by peptide bonds
in a specific sequence to form distinct proteins
• amino acids contain C, O, H, N, and sometimes sulphur
or phosphorous

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Introduction
Amino acid structure contains: amine group (NH2),
carboxylic group (COOH), side chain (R group)

Structure
Structure of some amino acids
• amino acids differ in composition of side chain
• side chains distinguish the physical and chemical
properties of amino acids

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Structure
Classification
• Essential amino acids (EAA): indispensable, cannot be
synthesised by human body (made out of materials ordinarily
available to the cells at a speed equal to the demands for
normal growth), must come from diet
• Non-essential amino acids (NEAA): dispensable, can be
synthesised by human body from diet and endogenous
amino acids
9 Essential amino acids 13 Non-essential amino acids
Histidine, Isoleucine, Alanine, Arginine, Asparagine,
Leucine, Lysine, Methionine, Aspartic acid, Cysteine,
Phenylalanine, Threonine, Glutamine, Glutamic acid,
Tryptophan, Valine Glycine, Proline, Serine, Tyrosine
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Structure
• Animal protein foods generally have higher
concentrations of essential amino acids (EAA) and in
adequate amounts than plant foods; referred as
complete proteins
• Plants lack some EAA, referred as incomplete
proteins; lysine is often the most limiting amino
acid, followed by sulphur-containing amino acids
(methionine, cystine), tryptophan and threonine

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Physiological role
I. Provide structure
builds structural components of organisms for growth
and maintenance (new tissues, repair)
• collagen, elastin, keratin, microtubules,
microfilaments
• matrix of collagen is filled with minerals to provide
strength to bones and teeth
• replaces worn-out tissues: skin, hair, nails, GIT lining
II. Provide energy
• 1 gram of protein contains 4 kcal
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Physiological role
III. Regulates body processes
1. enzymes (digestion, blood clotting, muscle contraction,
nerve transmission, energy production)
2. hormones (insulin, thyroid, etc)
3. carrier proteins (lipoproteins, haemoglobin+Oxygen, etc
4. antibodies (lymphocytes, immunity)
5. maintain water-electrolyte balance (plasma proteins
globulins & albumins exert pressure, transport sodium
ions out of cells and potassium ions into the cells
6. maintain acid-base balance (buffering action), accept and
release excess hydrogen ions due to its negative charge on
their surfaces 8

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Digestion, Absorption and Transport

Digestion (stomach, small intestine)
Hydrochloric acid:
unfolds structure of a protein (denaturation); protein
can be denatured outside the body by heat, acid,
alcohol, other chemicals
activates inactive proenzyme pepsinogen to active
enzyme pepsin which breaks long strands into small
chains of amino acids
chyme in the stomach move along to small intestine
for further digestion
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Digestion, Absorption and Transport

Digestion (stomach, small intestine)
Pancreatic proteases or proteolytic enzymes:
trypsin, chymotrypsin, carboxypeptidase break amino
acid strands into tripeptides, dipeptides & single amino
acids
Intestinal (brush border) enzymes (membrane bound to
the villi tips): peptidases (endopeptidase, dipeptidase,
aminopeptidase) produce single amino acids and
smaller peptides (di-, tri-) from tetrapeptides and
larger peptides
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Digestion, Absorption and Transport

Absorption and transportation
End products of digestion (free amino acids, di-
and tri-peptides) are absorbed across cell
membrane in the duodenum and jejunum by
specific carrier-mediated transporters through
the portal vein to the liver

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Utilisation
Amino acids in the cell can be used to:
• synthesise new protein
• provide nitrogen (amine groups to build non-essential
amino acids)
– e.g. metabolically indispensable amino acid glutamic
acid and glycine; they can be synthesised from
glucose and ammonium ions (to form glutamate)
and from carbon dioxide and ammonium ions (to
form glycine)
• provide energy if there is scarcity of energy nutrients
QN. Why does adequate energy spare protein (“protein
sparing”)? 12

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Utilisation
Unused amino acids are returned to the liver and
deaminated
• nitrogen portion is removed from amino acids,
converted to urea and excreted as urine via kidney
• non-nitrogenous portion is used to synthesise
glucose or fat, provide energy or can be stored as
energy reserve

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Utilisation
• Proteins are being continually synthesised and
degraded in a process referred to as turnover
Turnover (synthesis and breakdown associated with
tissue remodeling and repair, as well as removal of
abnormal proteins)
Protein synthesis and degradation are energy-requiring
processes (appr. 20% of total basal energy metabolism)
• Rate of turnover and balance of synthesis and
degradation of proteins, in addition to the mass of
protein, are important determinants of the
requirements for amino acids and nitrogen
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Utilisation
Adequate Protein synthesis requires:
1. presence of all essential amino acids in adequate
amounts; 2. adequate total amount of protein (to
supply amine groups that will synthesise the non-
essential amino acids) and 3. adequate energy-yielding
CHOs and fat (to spare the protein)
Amino acids are not used to build protein (wasted):
i. whenever there is not enough energy from CHOs, fat
ii. an imbalance due to inadequate essential amino acids,
protein of low-quality (incomplete)
iii. too much protein so that not all is needed e.g. too
much of any amino acid from a supplement 15

Utilisation
QNs. What does it mean by “limiting amino acid”?
What are consequences of lacking one EAA?
If any of the 9 EAA is absent, protein synthesis stops,
available/remaining AAs will be used for energy or
converted to fat and stored. Because the absence of
just one EAA halts protein synthesis, the EAA in
shortest supply in a food or diet becomes the
limiting factor (or limiting AA)
Food proteins complement each other by amino acids
contents i.e. protein complementation

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Dietary sources
Food proteins supply amino acids from which the
body makes its own proteins
• animal-source foods (milk, meat, & their products)
• legumes (beans, soybeans, peas, cowpeas, etc)
• nuts and oil seeds (groundnuts, sesame, etc)
• cereals (wheat, sorghum, millets, oats, maize, etc)
Protein contents differ between these sources
(check food composition tables)

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Dietary requirements
• Rate of protein synthesis is higher in young children
(& pregnant women) than adults: related to
deposition of protein during growth and high rate
of protein turnover (synthesis and breakdown)
associated with tissue remodelling, repair and
removal of abnormal proteins
• Rate in adults is considered to be sufficient to
achieve a “maintenance” level, decreasing gradually
in later years (due to decline in skeletal muscles);
Strength training can partially reverse this decline
and improve overall function
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Dietary requirements
RDA of high-quality reference protein for normal humans
Age (years) Weight (kg) RDA (g/kg/day)
4–6 20 1.1
7 – 10 28 1.0
11 – 14
Males 45 1.0
Females 46 1.0
15 – 18
Males 66 0.9
Females 55 0.8
19 +
Males 72-79 0.8
Females 58-65 0.8
Pregnancy + 10 (g/day)
Lactation (1st 6 months) +15 (g/day)
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Lactation (2nd 6 months) +12 (g/day)

Dietary requirements
Factors that affect protein and amino acid requirements
and nutritional status of individual
• Dietary (protein & amino acid source, resistance to
proteases; low energy intake; presence of anti-
nutritional factors in diet (bind enzymes trypsin, etc)
• Individual (age, sex, physical activity, genetics, drugs,
infections, physical trauma, chronic disease, cancer, etc)
• Environmental (physical: unsuitable housing,
inadequate heating; poor sanitary conditions)
• Socio-economic: poverty; dietary habits, food choices

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Dietary sources, requirements

How much protein did you consume yesterday?
• record food intake and ingredien. (morning to evening)
• check protein content of meals or individual food
items in food composition tables
https://www.hsph.harvard.edu/nutritionsource/food-
tables/
• calculate total protein intake
• compare to recommended daily intakes
• how much energy does this represent?
Calculating percentages energy from protein
Protein intake (g) x 4 kcal x 100
Total energy intake kcal
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Dietary sources, requirements

Example: protein intake (yesterday, 3-days, etc)
intake: stiff maize porridge ugali 190g, bean stew 110g
(beans 350g, onions 78g, tomatoes 90g, veg. oil 60g)
protein content per 100 g (found in food composition
tables, pages 24 & 72):
per meal? ugali 2.7g/100g, bean stew 4.9g/100g
per ingredients? maize flour? beans? onions? tomatoes?
veg. oil?
protein intake: ugali 2.7 x 190/100=5.13g; bean stew 4.9
x 110/100 =5.4g. Total 10.53g. recommendation??
energy intake from protein: 10.53 x 4 kcal=42.12 kcal
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Protein and health

Inadequate intake
• Failure in Physiological roles e.g. low antibodies,
hormones, enzymes, acid-base & water-electrolyte
imbalance, etc
Excess intake
• Gout (accumulation of uric acid as urate crystals in
joints due to excess intake of meats, alcohol)
• Liver, heart and kidney problems (overworked)
• Weight gain
Intolerance: consumption of gluten (protein found in
wheat, barley, rye) leads to damage of the small
intestine 23

Reading assignment
1. Concepts of Complete and Incomplete proteins
2. Not all proteins are created equal: concept of
animal vs. plant proteins, and protein
complementation
3. Methods of evaluating protein quality: Biological
Value, Net Protein Utilisation, Amino Acid Score,
Protein Efficiency Ratio, etc

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Questions? Clarification?

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